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Database: UniProt/SWISS-PROT
Entry: BGAL_OENOB
LinkDB: BGAL_OENOB
Original site: BGAL_OENOB 
ID   BGAL_OENOB              Reviewed;        1031 AA.
AC   Q04F24;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   19-FEB-2014, entry version 52.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=OEOE_1044;
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Oenococcus.
OX   NCBI_TaxID=203123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer (By similarity).
CC   -!- COFACTOR: Binds 1 sodium ion per monomer (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
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DR   EMBL; CP000411; ABJ56948.1; -; Genomic_DNA.
DR   RefSeq; YP_810613.1; NC_008528.1.
DR   ProteinModelPortal; Q04F24; -.
DR   STRING; 203123.OEOE_1044; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ABJ56948; ABJ56948; OEOE_1044.
DR   GeneID; 4415716; -.
DR   KEGG; ooe:OEOE_1044; -.
DR   PATRIC; 22800265; VBIOenOen113004_1059.
DR   eggNOG; COG3250; -.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; HRCAWDQ; -.
DR   OrthoDB; EOG6XWV0T; -.
DR   ProtClustDB; PRK09525; -.
DR   BioCyc; OOEN203123:GHNL-1044-MONOMER; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.320; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.80; -; 1.
DR   HAMAP; MF_01687; Beta_gal; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR011013; Gal_mutarotase_SF_dom.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosidase; Hydrolase; Magnesium; Metal-binding;
KW   Sodium.
FT   CHAIN         1   1031       Beta-galactosidase.
FT                                /FTId=PRO_0000367004.
FT   REGION      533    536       Substrate binding (By similarity).
FT   ACT_SITE    457    457       Proton donor (By similarity).
FT   ACT_SITE    533    533       Nucleophile (By similarity).
FT   METAL       197    197       Sodium (By similarity).
FT   METAL       412    412       Magnesium 1 (By similarity).
FT   METAL       414    414       Magnesium 1 (By similarity).
FT   METAL       457    457       Magnesium 1 (By similarity).
FT   METAL       593    593       Magnesium 2 (By similarity).
FT   METAL       597    597       Sodium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       600    600       Sodium (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     197    197       Substrate (By similarity).
FT   BINDING     457    457       Substrate (By similarity).
FT   BINDING     600    600       Substrate (By similarity).
FT   BINDING    1005   1005       Substrate (By similarity).
FT   SITE        353    353       Transition state stabilizer (By
FT                                similarity).
FT   SITE        387    387       Transition state stabilizer (By
FT                                similarity).
SQ   SEQUENCE   1031 AA;  118758 MW;  ABBC52BF9A20F31B CRC64;
     MTNKISFRDI INRKDWENPV ITNWHRLPIH TEMNYSKSLN EDKQKTIQSL NGNWCFSYFS
     KVTDVPENWA DRDLTKSNIM PVPSNWQLHG YDQPIYSNVA YPFPANPPYL PEENPTACYS
     RIFQLNDDWL QSGQNHVIFN GVGSAFHLWL NGQWIGYSED SRLPAEFDLT KYLKSGKNRI
     SVMVLRWSKG SYFEDQDMWR MSGIFRDVEV KHLPATYLQD YQLQTDLDDD LDQAKITIKA
     QVAGKNFSQN KLRTRLYFAN EKVADQSSRL STRAVDERGP LDNQFIAELN LKDPYLWSAE
     LPYLYQLVIE LLTDDGDILQ VEKVNIGVRK VEIKNGLLKL NGKPLLIRGT NKHEFDSKKG
     YAVDEETMIQ DIKAMKRNNF NAVRCSHYPN NRRWYELCDQ YGLYVVDEAN IETHGMVPMN
     RLTNDPVYLP LMSDRVTRMV TRDRNHPSII IWSLGNESGY GRNHAALYNW IKQSDLSRPV
     QYEGGGANTA VTDIIVPMYA RVEQDQIESV NSKWSLKKWI GLPGETRPLI LCEYAHDMGN
     SLGGFGKYWQ AFHKYPRLQG GFIWDWVDQG LLKKDVNGND FYAYGGDFKD QPNDRQFCLD
     GLLFPDRTPK PAMHEVKYWQ QYYLFNLQRN PLGQAESFTV TNDYSFKKSS NERLHYQIKS
     ENEIVIDKYI DLVLNPGESL LIKLPKGRSS TSSLLDIDIS LIKGNSWAPS GFKIASEQYV
     LAKKFGPTNA VTAATNKISL IENKDTNTFE IKLDDQKWQF AKNSGLLVSW SKSGNENLLD
     ALRDQFTRAP LDNDIGVSKV DHIDPNAWYE RWKSAGMYNL KTNLVSIDAE QLERAVLIRT
     EHSYSNHFQI LFKSSKIYRI DANGTMTVTV DVSLAQGIPF PARIGLTCHL ADQITDVSYT
     GLGPFENYPD RQSAAQYGHW QMELDDLYTP YIFPSENGSR GQVSQLEFGK QKISAYHEQN
     FSFNLSRFSK QQLARISHRN LLQAENGVWL SIDGYRMGVG GDDSWSPSVA PEYLLSNNYY
     HYAFQWCRKD I
//
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